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Cancer. 2008 Apr 25;114(2):124-33. doi: 10.1002/cncr.23349.

N-glycoprotein profiling of lung adenocarcinoma pleural effusions by shotgun proteomics.

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  • 1Institute for Surgical Pathology, University Hospital Zurich, Zurich Switzerland. alex.soltermann@usz.ch

Abstract

BACKGROUND:

Malignant pleural effusion of advanced lung adenocarcinoma may be a valid source for detection of biomarkers, such as N-glycosylated proteins (N-GP), because tumor cells grow during weeks in this liquid. The authors aimed for creation of N-GP effusion profiles from routine cytology specimens to detect relevant biomarkers.

METHODS:

Hundred microliters of malignant pleural effusions of 5 patients with lung adenocarcinoma and 5 nonmalignant controls were used for triplicate N-GP capture by solid-phase extraction. After trypsin digest and PNGase F release, a liquid chromatography separation connected online to a tandem mass spectrometer was performed by liquid chromatography/tandem mass spectrometry (LC/MS/MS).

RESULTS:

In the total of 10 samples, 170 and 278 nonredundant proteins were detected with probabilities of >or=.9 and >or=.5, respectively. The specificity for the N-glycomotif was 88% at P >or= .9. Penetration into the moderate to low protein concentration range (microg-ng/mL) occurred, and several proteins associated with tumor progression or metastasis were identified, including CA-125, CD44, CD166, lysosome-associated membrane glycoprotein 2 (LAMP-2), multimerin 2, and periostin. MS identifications were correlated with the corresponding immunoreactivity in either effusion fluid or tumor tissue.

CONCLUSIONS:

In conclusion, reduction of sample complexity by N-GP capturing allows detection of proteins in the mug to ng/mL range. Pleural effusion is a useful source for biomarker research in lung cancer.

Copyright (c) American Cancer Society.

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